Membrane protein crystallization from lipidic phases
Artikel i vetenskaplig tidskrift, 2009

Membrane protein structural biology is enjoying a steady acceleration in the rate of success. Nevertheless, numerous membrane protein targets are resistant to the traditional approach of directly crystallizing detergent solubilized and purified protein and the 'niche market' of lipidic phase crystallization is emerging as a powerful complement. These approaches, including lipidic cubic phase, lipidic sponge phase, and bicelle crystallization methods, all immerse purified membrane protein within a lipid rich matrix before crystallization. This environment is hypothesized to contribute to the protein's long-term structural stability and thereby favor crystallization. Spectacular recent successes include the high-resolution structures of the beta(2)-adrenergic G-protein-coupled receptor, the A(2A) adenosine G-protein-coupled receptor, and the mitochondrial voltage dependent anion channel. In combination with technical innovations aiming to popularize these methods, lipidic phase crystallization approaches can be expected to deliver an increasing scientific impact as the field develops.

Författare

Linda C Johansson

Göteborgs universitet

Annemarie Wöhri

Chalmers, Kemi- och bioteknik, Molekylär mikroskopi

Gergely Katona

Göteborgs universitet

Sven Engström

Chalmers, Kemi- och bioteknik, Teknisk ytkemi

Richard Neutze

Göteborgs universitet

Current Opinion in Structural Biology

0959-440X (ISSN)

Vol. 19 372-378

Ämneskategorier

Annan kemi

DOI

10.1016/j.sbi.2009.05.006